ID GLO5_ORYSJ Reviewed; 369 AA. AC Q6YT73; A0A0P0X2P6; B9FVJ4; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 10-APR-2019, entry version 110. DE RecName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase GLO5; DE EC=1.1.3.15; DE AltName: Full=Glycolate oxidase 5; DE Short=GOX 5; DE Short=OsGLO5; DE AltName: Full=Short chain alpha-hydroxy acid oxidase GLO5; GN Name=GLO5; OrderedLocusNames=Os07g0152900, LOC_Os07g05820; GN ORFNames=B1364A02.33-1, OsJ_23125, OSJNBb0050B07.1-1; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., RA McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., RA Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L., RA Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T., RA Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using RT next generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). RN [6] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=19264754; DOI=10.1093/jxb/erp056; RA Xu H.-W., Zhang J., Zeng J., Jiang L., Liu E., Peng C., He Z.-H., RA Peng X.-X.; RT "Inducible antisense suppression of glycolate oxidase reveals its RT strong regulation over photosynthesis in rice."; RL J. Exp. Bot. 60:1799-1809(2009). CC -!- FUNCTION: Photorespiratory enzyme that can exert a strong CC regulation over photosynthesis, possibly through a feed-back CC inhibition on Rubisco activase. Not required for oxalate CC accumulation (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + CC H2O2; Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; CC EC=1.1.3.15; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00683}; CC -!- PATHWAY: Photosynthesis; photorespiration; glycine from 2- CC phosphoglycolate: step 2/3. CC -!- SUBUNIT: Homotetramer or homooctamer. Interacts with rice dwarf CC virus (RDV) P8. This interaction promotes viral P8 relocation to CC virus factories peripheral to peroxisomes (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP005632; BAD31578.1; -; Genomic_DNA. DR EMBL; AP006163; BAC84719.1; -; Genomic_DNA. DR EMBL; AP008213; BAF20823.1; -; Genomic_DNA. DR EMBL; AP014963; BAT00100.1; -; Genomic_DNA. DR EMBL; CM000144; EEE66581.1; -; Genomic_DNA. DR EMBL; AK062189; BAG88242.1; -; mRNA. DR EMBL; AK103933; BAG96328.1; -; mRNA. DR RefSeq; XP_015646859.1; XM_015791373.1. DR UniGene; Os.51287; -. DR ProteinModelPortal; Q6YT73; -. DR SMR; Q6YT73; -. DR STRING; 4530.OS07T0152900-01; -. DR PaxDb; Q6YT73; -. DR PRIDE; Q6YT73; -. DR EnsemblPlants; Os07t0152900-01; Os07t0152900-01; Os07g0152900. DR EnsemblPlants; Os07t0152900-03; Os07t0152900-03; Os07g0152900. DR EnsemblPlants; Os07t0152900-04; Os07t0152900-04; Os07g0152900. DR GeneID; 4342420; -. DR Gramene; Os07t0152900-01; Os07t0152900-01; Os07g0152900. DR Gramene; Os07t0152900-03; Os07t0152900-03; Os07g0152900. DR Gramene; Os07t0152900-04; Os07t0152900-04; Os07g0152900. DR KEGG; osa:4342420; -. DR eggNOG; KOG0538; Eukaryota. DR eggNOG; COG1304; LUCA. DR InParanoid; Q6YT73; -. DR KO; K11517; -. DR OMA; KSVYDYY; -. DR OrthoDB; 879633at2759; -. DR Reactome; R-OSA-389661; Glyoxylate metabolism and glycine degradation. DR Reactome; R-OSA-390918; Peroxisomal lipid metabolism. DR UniPathway; UPA00951; UER00912. DR Proteomes; UP000059680; Chromosome 7. DR ExpressionAtlas; Q6YT73; differential. DR Genevisible; Q6YT73; OS. DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB. DR GO; GO:0010181; F:FMN binding; IBA:GO_Central. DR GO; GO:0008891; F:glycolate oxidase activity; ISS:UniProtKB. DR GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; ISS:UniProtKB. DR GO; GO:0009854; P:oxidative photosynthetic carbon pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0009853; P:photorespiration; ISS:UniProtKB. DR GO; GO:0010109; P:regulation of photosynthesis; ISS:UniProtKB. DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR037396; FMN_HAD. DR InterPro; IPR008259; FMN_hydac_DH_AS. DR Pfam; PF01070; FMN_dh; 1. DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Flavoprotein; FMN; Glycolate pathway; KW Host-virus interaction; Oxidoreductase; Peroxisome; Photorespiration; KW Reference proteome. FT CHAIN 1 369 Peroxisomal (S)-2-hydroxy-acid oxidase FT GLO5. FT /FTId=PRO_0000403417. FT DOMAIN 1 360 FMN hydroxy acid dehydrogenase. FT {ECO:0000255|PROSITE-ProRule:PRU00683}. FT NP_BIND 286 310 FMN. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT MOTIF 367 369 Microbody targeting signal. FT {ECO:0000255}. FT ACT_SITE 255 255 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT BINDING 25 25 Substrate. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT BINDING 107 107 FMN. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT BINDING 128 128 FMN. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT BINDING 130 130 Substrate. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT BINDING 156 156 FMN. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT BINDING 165 165 Substrate. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT BINDING 231 231 FMN. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT BINDING 258 258 Substrate. {ECO:0000255|PROSITE- FT ProRule:PRU00683}. FT CONFLICT 265 265 A -> S (in Ref. 4; EEE66581). FT {ECO:0000305}. SQ SEQUENCE 369 AA; 40245 MW; FE652FD1115F2681 CRC64; MGEITNVTEY QAIAKQKLPK MIYDYYASGA EDEWTLQENR EAFARILFRP RILIDVSKID MATTVLGFKI SMPIMIAPSA MQKMAHPDGE YATARAASAA GTIMTLSSWA TSSVEEVAST GPGIRFFQLY VYKDRRVVEQ LVRRAERAGF KAIALTVDTP RLGRREADIK NRFVLPPFLT LKNFEGLELG KMDQASDSGL ASYVAGQIDR TLSWKDVKWL QTITTLPILV KGVITAEDTR LAVENGAAGI IVSNHGARQL DYVPATISAL EEVVKAARGQ LPVFLDGGVR RGTDVFKALA LGAAGVFIGR PVVFSLAAAG EAGVRNVLQM LRDEFELTMA LSGCTSLADI TRNHVITEAD KLGVMPSRL //